PIOX_PEA
ID PIOX_PEA Reviewed; 643 AA.
AC Q5GQ66;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Alpha-dioxygenase PIOX {ECO:0000305};
DE EC=1.13.11.92 {ECO:0000269|PubMed:10938370};
DE AltName: Full=Pathogen-induced oxygenase {ECO:0000303|PubMed:10938370};
GN Name=alphaDOX1 {ECO:0000303|PubMed:18760499};
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18760499; DOI=10.1016/j.jplph.2008.05.009;
RA Meisner A.K., Saffert A., Schreier P., Schoen A.;
RT "Fatty acid alpha-dioxygenase from Pisum sativum: temporal and spatial
RT regulation during germination and plant development.";
RL J. Plant Physiol. 166:333-343(2009).
RN [2]
RP PROTEIN SEQUENCE OF 447-457 AND 567-575, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10938370; DOI=10.1104/pp.123.4.1545;
RA Saffert A., Hartmann-Schreier J., Schoen A., Schreier P.;
RT "A dual function alpha-dioxygenase-peroxidase and NAD(+) oxidoreductase
RT active enzyme from germinating pea rationalizing alpha-oxidation of fatty
RT acids in plants.";
RL Plant Physiol. 123:1545-1552(2000).
CC -!- FUNCTION: Alpha-dioxygenase that catalyzes the primary oxygenation step
CC of a variety of 14-20 carbon fatty acids, containing up to three
CC unsaturated bonds, into their corresponding 2R-hydroperoxides
CC (PubMed:18760499, PubMed:10938370). Involved in the production of
CC oxylipins that function in cell signaling, wound healing, and
CC protection from infection (PubMed:18760499, PubMed:10938370). The
CC alpha-oxidation pathway of fatty acids may play a role during plant
CC developmental processes (PubMed:18760499).
CC {ECO:0000269|PubMed:10938370, ECO:0000269|PubMed:18760499}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate + O2 = (2R)-2-hydroperoxyhexadecanoate;
CC Xref=Rhea:RHEA:63836, ChEBI:CHEBI:7896, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:149616; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:10938370};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63837;
CC Evidence={ECO:0000269|PubMed:10938370};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + O2 = (2R)-2-hydroperoxydodecanoate;
CC Xref=Rhea:RHEA:63852, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:149611; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:10938370};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63853;
CC Evidence={ECO:0000269|PubMed:10938370};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q9SGH6};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250|UniProtKB:Q9SGH6};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9SGH6};
CC Note=Binds 1 calcium ion per subunit. {ECO:0000250|UniProtKB:Q9SGH6};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 uM for O2 {ECO:0000269|PubMed:10938370};
CC KM=55 uM for dodecanoate {ECO:0000269|PubMed:10938370};
CC -!- DEVELOPMENTAL STAGE: Expressed in germinating seeds and then root
CC seedlings up to 12 days after imbibition.
CC {ECO:0000269|PubMed:18760499}.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00298}.
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DR EMBL; AJ784963; CAH05011.1; -; mRNA.
DR SMR; Q5GQ66; -.
DR PeroxiBase; 5968; PsDiOx01.
DR KEGG; ag:CAH05011; -.
DR BioCyc; MetaCyc:MON-5641; -.
DR BRENDA; 1.13.11.92; 4872.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09818; PIOX_like; 1.
DR Gene3D; 1.10.640.10; -; 1.
DR InterPro; IPR034815; A_dioxygenase.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR Pfam; PF03098; An_peroxidase; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW Calcium; Dioxygenase; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Oxylipin biosynthesis; Peroxidase;
KW Plant defense.
FT CHAIN 1..643
FT /note="Alpha-dioxygenase PIOX"
FT /id="PRO_0000455383"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 173
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 393
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 490
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 494
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT SITE 270
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
SQ SEQUENCE 643 AA; 73297 MW; E861179E04F9686B CRC64;
MWSIVTDPIK DLISKVVKNS IHPDFHDAVS KMTIIDAFLF FIVHSIDKLG IWHRLPVFFG
LLYLAIRRHL HQEYNLLNVG TTPVGIRSNP SDFPYRTADG RYNDPFNDGA GSQGSFFGRN
ILPVDQKNKL LKPDPMVVVT KLLERKTYKD TGTQFNVIAA SWIQFMIHDW IDHMEDTKQV
ELSAPSEVAS QCPLKSFKFF KTKEIPTGFY DIKTGHANVR TPWWDGSVVY GSNEQVLNKV
RTFKDGKLKI SKEGHLLHNE DGTAISGDIR NSWAGVTTLQ TLFVQEHNAV CDALKKENSD
LEDEDLYRHA RLVTSAVIAK IHTIDWTVEL LKTDTLLAGM RANWYGLLGK QFKDRFGHVG
NSILSGFVGM KRSENHGVPY SLTEEFATVY RMHPLLPDSL HLRDISASPG PNKSPPLIKE
IPMNDLIGLQ GEKTLLEIGN AKKLVSMGHQ ACGALELWNY PSWLRNLVPH NIDGTERSDH
VDLAALEVYR DRERNVARYN QFRRGLLLIP ISKWEDLTDD EEAIKVLEEV YGDDVEELDV
LVGLMAEKKI KGFAISETAF VIFLLMASRR LEADRFFTSN FNEETYTKKG LEWVNTTESL
KDVIDRHHPE MTHKWLNSSS AFSVWDTSPN KHNHIPIYFR VPN
